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Literature summary for 1.1.1.184 extracted from

  • Moschini, R.; Peroni, E.; Rotondo, R.; Renzone, G.; Melck, D.; Cappiello, M.; Srebot, M.; Napolitano, E.; Motta, A.; Scaloni, A.; Mura, U.; Del-Corso, A.
    NADP(+)-dependent dehydrogenase activity of carbonyl reductase on glutathionylhydroxynonanal as a new pathway for hydroxynonenal detoxification (2015), Free Radic. Biol. Med., 83, 66-76.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.033
-
3-glutathionyl-4-hydroxynonanal pH 8.4, 37°C Homo sapiens

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
31000
-
x * 31000, SDS-PAGE Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Storage Stability

Storage Stability Organism
4°C, 0.1 mM NADP+, 1.5 M NaCl, stable for at least 2 weeks Homo sapiens

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3-glutathionyl-4-hydroxynonanal + NADPH + H+
-
Homo sapiens 3-glutathionyl-1,4-dihydroxynonane + NADP+
-
?
4-oxo-2-nonenal + NADPH + H+ 9% of the activity with 9,10-phenanthrenequinone Homo sapiens ? + NADP+
-
?
9,10-phenanthrenequinone + NADPH + H+
-
Homo sapiens ? + NADP+
-
?
menadione + NADPH + H+ 48% of the activity with 9,10-phenanthrenequinone Homo sapiens ? + NADP+
-
?
additional information carbonyl reductase oxidizes the hydroxyl group of 3-glutathionyl-4-hydroxynonanal in its hemiacetal form, with the formation of the corresponding 3-glutathionyl nonanoic-delta-lactone. The enzyme is practically inactive toward trans-4-hydroxy-2-nonenal, buthionine sulfoximine, N-acetylcysteine Homo sapiens ?
-
?

Subunits

Subunits Comment Organism
? x * 31000, SDS-PAGE Homo sapiens

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
6.75
-
3-glutathionyl-4-hydroxynonanal pH 8.4, 37°C Homo sapiens

Cofactor

Cofactor Comment Organism Structure
additional information no cofactor: NADH Homo sapiens
NADPH
-
Homo sapiens